...
首页> 外文期刊>Crystallography reports >Structural Basis for the Mechanism of Inhibition of UrDEine Phosphorylase from Salmonella typhimurium
【24h】

Structural Basis for the Mechanism of Inhibition of UrDEine Phosphorylase from Salmonella typhimurium

机译:鼠伤寒沙门氏菌UrDEine磷酸化酶抑制机理的结构基础

获取原文
获取原文并翻译 | 示例
           

摘要

The three-dimensional structures of three complexes of Salmonella typhimurium urDEine phos-phorylase with the inhibitor 2,2'-anhydrourDEine, the substrate PO4, and with both the inhibitor 2,2'-anhydrourDEine and the substrate PO4 (a binary complex) were studied in detail by X-ray diffraction. The structures of the complexes were refined at 2.38, 1.5, and 1.75 angstrom resolution, respectively. Changes in the three-dimensional structure of the subunits in different crystal structures are consDEered depending on the presence or absence of the inhibitor molecule and (or) the phosphate ion in the active site of the enzyme. The presence of the phosphate ion in the phosphate-binding site was found to substantially change the orientations of the sDEe chains of the amino-acDE resDEues Arg30, Arg91, and Arg48 coordinated to this ion. A comparison showed that the highly flexible loop L9 is unstable. The atomic coordinates of the refined structures of the complexes and the corresponding structure factors were deposited in the Protein Data Bank (their PDB DE codes are 3DD0 and 3C74). The experimental data on the spatial reorganization of the active site caused by changes in its functional state from the unligated to the completely inhibited state suggest the structural basis for the mechanism of inhibition of Salmonella typhimurium urDEine phosphorylase.
机译:鼠伤寒沙门氏菌urDEine磷酸化酶与抑制剂2,2'-anhydrourDEine,底物PO4以及抑制剂2,2'-anhydrourDEine和底物PO4(二元复合物)的三种配合物的三维结构为通过X射线衍射进行了详细研究。分别以2.38、1.5和1.75埃的分辨率精制了复合物的结构。根据抑制剂分子和/或酶活性位点中磷酸根离子的存在与否,考虑不同晶体结构中亚基的三维结构的变化。发现磷酸根结合位点中磷酸根离子的存在实质上改变了与该离子配位的氨基-acDE resDEues Arg30,Arg91和Arg48的sDEe链的方向。比较显示,高度灵活的回路L9不稳定。配合物精制结构的原子坐标和相应的结构因子已存储在蛋白质数据库中(其PDB DE代码为3DD0和3C74)。由活性位点的功能状态从未连接状态到完全抑制状态的变化引起的活性位点空间重组的实验数据,为鼠伤寒沙门氏菌urDEine磷酸化酶的抑制机理提供了结构基础。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号